Crystal structure of the trithorax group protein ASH2L reveals a forkhead-like DNA binding domain - Wikidata - awgldk - TriplyDB

Crystal structure of the trithorax group protein ASH2L reveals a forkhead-like DNA binding domain

Crystal structure of the trithorax group protein ASH2L reveals a forkhead-like DNA binding domain

http://www.wikidata.org/entity/Q27666253

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Hijacked in cancer: the KMT2 (MLL) family of methyltransferases The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases Molecular basis for DPY-30 association to COMPASS-like and NURF complexes A non-active-site SET domain surface crucial for the interaction of MLL1 and the RbBP5/Ash2L heterodimer within MLL family core complexes Substrate and product specificities of SET domain methyltransferases Trithorax group proteins: switching genes on and keeping them active.WRAD: enabler of the SET1-family of H3K4 methyltransferases.Absent, small or homeotic 2-like protein (ASH2L) enhances the transcription of the estrogen receptor α gene through GATA-binding protein 3 (GATA3).A phosphorylation switch on RbBP5 regulates histone H3 Lys4 methylation.The Cardiac Stress Response Factor Ms1 Can Bind to DNA and Has a Function in the Nucleus The trithorax group protein Ash2l is essential for pluripotency and maintaining open chromatin in embryonic stem cells.SET for life: biochemical activities and biological functions of SET domain-containing proteins The many facets of MLL1 regulation.The interaction of MYC with the trithorax protein ASH2L promotes gene transcription by regulating H3K27 modification.Xist RNA repeat E is essential for ASH2L recruitment to the inactive X and regulates histone modifications and escape gene expression.CpG island structure and trithorax/polycomb chromatin domains in human cells DNA binding by PHF1 prolongs PRC2 residence time on chromatin and thereby promotes H3K27 methylation.Low expression of ASH2L protein correlates with a favorable outcome in acute myeloid leukemia.Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin.

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P2860

Crystal structure of the trithorax group protein ASH2L reveals a forkhead-like DNA binding domain

http://www.wikidata.org/entity/Q27666253

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Crystal structure of the trith ...... rkhead-like DNA binding domain

@ast

Crystal structure of the trith ...... rkhead-like DNA binding domain

@en

Crystal structure of the trith ...... rkhead-like DNA binding domain

@nl

type

label

Crystal structure of the trith ...... rkhead-like DNA binding domain

@ast

Crystal structure of the trith ...... rkhead-like DNA binding domain

@en

Crystal structure of the trith ...... rkhead-like DNA binding domain

@nl

prefLabel

Crystal structure of the trith ...... rkhead-like DNA binding domain

@ast

Crystal structure of the trith ...... rkhead-like DNA binding domain

@en

Crystal structure of the trith ...... rkhead-like DNA binding domain

@nl

P1433

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P1433

Nature Structural & Molecular Biology

P1476

Crystal structure of the trith ...... rkhead-like DNA binding domain

@en

P2093

Alexandre Blais

http://www.w3.org/2001/XMLSchema#string

Chandra-Prakash Chaturvedi

http://www.w3.org/2001/XMLSchema#string

Jean-François Couture

http://www.w3.org/2001/XMLSchema#string

Joseph S Brunzelle

http://www.w3.org/2001/XMLSchema#string

Marjorie Brand

http://www.w3.org/2001/XMLSchema#string

Pamela Zhang

http://www.w3.org/2001/XMLSchema#string

Sabina Sarvan

http://www.w3.org/2001/XMLSchema#string

Sylvain Lanouette

http://www.w3.org/2001/XMLSchema#string

Vanja Avdic

http://www.w3.org/2001/XMLSchema#string

Véronique Tremblay

http://www.w3.org/2001/XMLSchema#string

P2860

Structural Basis for DNA Recognition by FoxO1 and Its Regulation by Posttranslational Modification

Structural and biochemical insights into MLL1 core complex assembly

Searching protein structure databases with DaliLite v.3

Regulation of MLL1 H3K4 methyltransferase activity by its core components

An Ash2L/RbBP5 heterodimer stimulates the MLL1 methyltransferase activity through coordinated substrate interactions with the MLL1 SET domain

p38 MAPK signaling regulates recruitment of Ash2L-containing methyltransferase complexes to specific genes during differentiation.

Molecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes.

Activator-mediated recruitment of the MLL2 methyltransferase complex to the beta-globin locus.

Transcription factor Ap2delta associates with Ash2l and ALR, a trithorax family histone methyltransferase, to activate Hoxc8 transcription

Structure/function relationships underlying regulation of FOXO transcription factors.

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857-9

http://www.w3.org/2001/XMLSchema#string

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scholarly article

P356

10.1038/NSMB.2093

http://www.w3.org/2001/XMLSchema#string

P433

7

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18

http://www.w3.org/2001/XMLSchema#string

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2011-06-05T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

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51193201

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P6179

1047506745

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P698

21642971

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P921

protein structure

crystal structure

structural biology

P932

3983046

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